FMO DATABASE

FMODB ID: 52MNZ

Calculation Name: 1NXM-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1NXM

Chain ID: A

ChEMBL ID:

UniProt ID: Q8GIQ0

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	194
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2231202.892285
FMO2-HF: Nuclear repulsion	2155081.208193
FMO2-HF: Total energy	-76121.684093
FMO2-MP2: Total energy	-76349.132376

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASN)

Summations of interaction energy for fragment #1(A:4:ASN)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-7.268	-3.793	1.196	-1.852	-2.817	0.011

Interaction energy analysis for fragmet #1(A:4:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.019 / q_NPA : -0.029

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	6	PHE	0	0.029	0.005	3.867	-1.767	0.200	-0.023	-1.002	-0.941	-0.002
4	A	7	GLY	0	-0.027	-0.015	5.016	1.338	1.404	-0.001	-0.002	-0.062	0.000
5	A	8	LYS	1	0.777	0.912	2.460	-7.072	-5.674	1.221	-0.846	-1.773	0.013
6	A	9	THR	0	0.000	-0.014	6.751	-0.868	-0.868	0.000	0.000	0.000	0.000
7	A	10	LEU	0	-0.015	0.003	8.676	0.201	0.201	0.000	0.000	0.000	0.000
8	A	11	ALA	0	-0.009	-0.003	9.100	-0.139	-0.139	0.000	0.000	0.000	0.000
9	A	12	ALA	0	0.023	0.010	10.977	-0.045	-0.045	0.000	0.000	0.000	0.000
10	A	13	ARG	1	0.785	0.863	5.661	-0.090	-0.090	0.000	0.000	0.000	0.000
11	A	14	PRO	0	0.015	0.002	12.088	-0.094	-0.094	0.000	0.000	0.000	0.000
12	A	15	VAL	0	-0.004	0.007	12.884	-0.059	-0.059	0.000	0.000	0.000	0.000
13	A	16	GLU	-1	-0.956	-0.978	15.252	-0.304	-0.304	0.000	0.000	0.000	0.000
14	A	17	ALA	0	0.009	0.014	17.493	0.034	0.034	0.000	0.000	0.000	0.000
15	A	18	ILE	0	0.006	0.002	18.336	0.025	0.025	0.000	0.000	0.000	0.000
16	A	19	PRO	0	0.033	0.018	19.719	0.026	0.026	0.000	0.000	0.000	0.000
17	A	20	GLY	0	0.016	0.004	20.594	0.006	0.006	0.000	0.000	0.000	0.000
18	A	21	MET	0	0.004	0.014	15.512	0.005	0.005	0.000	0.000	0.000	0.000
19	A	22	LEU	0	-0.043	-0.009	14.751	0.005	0.005	0.000	0.000	0.000	0.000
20	A	23	GLU	-1	-0.725	-0.824	7.339	-1.601	-1.601	0.000	0.000	0.000	0.000
21	A	24	PHE	0	0.014	-0.014	10.571	0.127	0.127	0.000	0.000	0.000	0.000
22	A	25	ASP	-1	-0.816	-0.872	5.134	2.211	2.255	-0.001	-0.002	-0.041	0.000
23	A	26	ILE	0	-0.008	-0.023	7.929	-0.102	-0.102	0.000	0.000	0.000	0.000
24	A	27	PRO	0	-0.011	-0.008	8.453	0.380	0.380	0.000	0.000	0.000	0.000
25	A	28	VAL	0	-0.008	0.011	8.325	-0.460	-0.460	0.000	0.000	0.000	0.000
26	A	29	HIS	0	-0.004	-0.001	9.098	0.627	0.627	0.000	0.000	0.000	0.000
27	A	30	GLY	0	0.029	-0.005	11.336	-0.306	-0.306	0.000	0.000	0.000	0.000
28	A	31	ASP	-1	-0.778	-0.853	10.240	1.095	1.095	0.000	0.000	0.000	0.000
29	A	32	ASN	0	0.003	-0.013	10.596	-0.055	-0.055	0.000	0.000	0.000	0.000
30	A	33	ARG	1	0.790	0.858	11.844	-0.754	-0.754	0.000	0.000	0.000	0.000
31	A	34	GLY	0	0.002	0.009	14.136	-0.096	-0.096	0.000	0.000	0.000	0.000
32	A	35	TRP	0	-0.030	-0.014	11.769	0.188	0.188	0.000	0.000	0.000	0.000
33	A	36	PHE	0	-0.008	0.000	14.120	-0.124	-0.124	0.000	0.000	0.000	0.000
34	A	37	LYS	1	0.821	0.886	12.512	-0.254	-0.254	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.879	-0.950	14.643	0.605	0.605	0.000	0.000	0.000	0.000
36	A	39	ASN	0	-0.027	-0.016	14.889	0.069	0.069	0.000	0.000	0.000	0.000
37	A	40	PHE	0	0.049	0.014	15.910	-0.046	-0.046	0.000	0.000	0.000	0.000
38	A	41	GLN	0	-0.022	-0.015	17.941	-0.032	-0.032	0.000	0.000	0.000	0.000
39	A	42	LYS	1	0.854	0.918	19.636	-0.166	-0.166	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-0.865	-0.916	22.171	0.462	0.462	0.000	0.000	0.000	0.000
41	A	44	LYS	1	0.828	0.905	17.714	-0.628	-0.628	0.000	0.000	0.000	0.000
42	A	45	MET	0	-0.025	0.008	16.136	0.048	0.048	0.000	0.000	0.000	0.000
43	A	46	LEU	0	-0.026	0.003	18.686	-0.031	-0.031	0.000	0.000	0.000	0.000
44	A	47	PRO	0	-0.032	-0.020	20.082	-0.028	-0.028	0.000	0.000	0.000	0.000
45	A	48	LEU	0	-0.058	-0.015	14.160	0.009	0.009	0.000	0.000	0.000	0.000
46	A	49	GLY	0	0.019	0.012	17.003	-0.024	-0.024	0.000	0.000	0.000	0.000
47	A	50	PHE	0	-0.019	-0.006	18.186	-0.050	-0.050	0.000	0.000	0.000	0.000
48	A	51	PRO	0	0.014	0.018	20.110	0.012	0.012	0.000	0.000	0.000	0.000
49	A	52	GLU	-1	-0.722	-0.869	23.586	0.156	0.156	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.022	-0.014	26.535	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	54	PHE	0	-0.035	-0.010	23.695	-0.011	-0.011	0.000	0.000	0.000	0.000
52	A	55	PHE	0	0.040	-0.011	23.995	0.001	0.001	0.000	0.000	0.000	0.000
53	A	56	ALA	0	-0.031	-0.005	28.920	0.002	0.002	0.000	0.000	0.000	0.000
54	A	57	GLU	-1	-0.842	-0.910	32.025	0.010	0.010	0.000	0.000	0.000	0.000
55	A	58	GLY	0	-0.060	-0.031	32.429	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.746	0.872	31.486	0.002	0.002	0.000	0.000	0.000	0.000
57	A	60	LEU	0	-0.016	-0.011	25.772	0.010	0.010	0.000	0.000	0.000	0.000
58	A	61	GLN	0	-0.022	-0.011	27.759	0.002	0.002	0.000	0.000	0.000	0.000
59	A	62	ASN	0	-0.073	-0.050	22.669	0.020	0.020	0.000	0.000	0.000	0.000
60	A	63	ASN	0	0.027	0.035	24.540	0.016	0.016	0.000	0.000	0.000	0.000
61	A	64	VAL	0	0.003	-0.015	22.374	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	65	SER	0	-0.022	-0.010	22.148	0.001	0.001	0.000	0.000	0.000	0.000
63	A	66	PHE	0	0.009	0.006	20.685	-0.028	-0.028	0.000	0.000	0.000	0.000
64	A	67	SER	0	-0.049	-0.030	21.575	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	68	ARG	1	0.878	0.929	21.082	0.246	0.246	0.000	0.000	0.000	0.000
66	A	69	LYS	1	0.877	0.909	17.590	0.573	0.573	0.000	0.000	0.000	0.000
67	A	70	ASN	0	-0.018	0.000	20.028	0.001	0.001	0.000	0.000	0.000	0.000
68	A	71	VAL	0	-0.042	0.000	21.711	0.006	0.006	0.000	0.000	0.000	0.000
69	A	72	LEU	0	0.005	0.009	21.156	-0.056	-0.056	0.000	0.000	0.000	0.000
70	A	73	ARG	1	0.791	0.898	22.233	0.344	0.344	0.000	0.000	0.000	0.000
71	A	74	GLY	0	0.025	0.015	22.518	-0.038	-0.038	0.000	0.000	0.000	0.000
72	A	75	LEU	0	-0.022	0.011	21.465	0.005	0.005	0.000	0.000	0.000	0.000
73	A	76	HIS	0	-0.049	-0.061	24.494	0.030	0.030	0.000	0.000	0.000	0.000
74	A	77	ALA	0	-0.008	0.015	24.904	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	78	GLU	-1	-0.758	-0.848	26.362	-0.114	-0.114	0.000	0.000	0.000	0.000
76	A	79	PRO	0	0.001	0.003	27.945	0.000	0.000	0.000	0.000	0.000	0.000
77	A	80	TRP	0	-0.055	-0.048	26.426	0.022	0.022	0.000	0.000	0.000	0.000
78	A	81	ASP	-1	-0.818	-0.881	23.661	-0.064	-0.064	0.000	0.000	0.000	0.000
79	A	82	LYS	1	0.820	0.889	20.843	0.178	0.178	0.000	0.000	0.000	0.000
80	A	83	TYR	0	0.015	0.015	14.807	0.006	0.006	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.010	0.000	15.584	0.029	0.029	0.000	0.000	0.000	0.000
82	A	85	SER	0	-0.002	-0.011	14.150	0.056	0.056	0.000	0.000	0.000	0.000
83	A	86	VAL	0	0.020	0.022	13.122	-0.056	-0.056	0.000	0.000	0.000	0.000
84	A	87	ALA	0	-0.009	-0.012	14.659	0.128	0.128	0.000	0.000	0.000	0.000
85	A	88	ASP	-1	-0.802	-0.910	15.862	-0.124	-0.124	0.000	0.000	0.000	0.000
86	A	89	GLY	0	-0.027	-0.021	12.309	0.013	0.013	0.000	0.000	0.000	0.000
87	A	90	GLY	0	0.018	0.015	12.302	-0.106	-0.106	0.000	0.000	0.000	0.000
88	A	91	LYS	1	0.812	0.898	9.862	1.556	1.556	0.000	0.000	0.000	0.000
89	A	92	VAL	0	0.007	-0.007	12.219	0.126	0.126	0.000	0.000	0.000	0.000
90	A	93	LEU	0	0.016	0.019	12.277	-0.228	-0.228	0.000	0.000	0.000	0.000
91	A	94	GLY	0	0.004	0.003	13.026	0.176	0.176	0.000	0.000	0.000	0.000
92	A	95	THR	0	0.005	0.003	14.384	-0.150	-0.150	0.000	0.000	0.000	0.000
93	A	96	TRP	0	-0.040	-0.035	13.198	0.051	0.051	0.000	0.000	0.000	0.000
94	A	97	VAL	0	0.050	0.021	19.235	-0.037	-0.037	0.000	0.000	0.000	0.000
95	A	98	ASP	-1	-0.766	-0.835	22.300	-0.187	-0.187	0.000	0.000	0.000	0.000
96	A	99	LEU	0	0.026	0.020	24.014	0.003	0.003	0.000	0.000	0.000	0.000
97	A	100	ARG	1	0.760	0.849	23.051	0.203	0.203	0.000	0.000	0.000	0.000
98	A	101	GLU	-1	-0.866	-0.945	28.944	-0.129	-0.129	0.000	0.000	0.000	0.000
99	A	102	GLY	0	-0.030	-0.036	30.208	0.017	0.017	0.000	0.000	0.000	0.000
100	A	103	GLU	-1	-0.958	-0.981	28.855	-0.150	-0.150	0.000	0.000	0.000	0.000
101	A	104	THR	0	-0.022	-0.020	24.121	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	105	PHE	0	-0.047	-0.003	25.392	-0.026	-0.026	0.000	0.000	0.000	0.000
103	A	106	GLY	0	0.026	0.003	26.263	0.001	0.001	0.000	0.000	0.000	0.000
104	A	107	ASN	0	-0.056	-0.019	21.559	-0.035	-0.035	0.000	0.000	0.000	0.000
105	A	108	THR	0	-0.044	-0.037	19.431	0.017	0.017	0.000	0.000	0.000	0.000
106	A	109	TYR	0	-0.038	-0.042	9.608	-0.023	-0.023	0.000	0.000	0.000	0.000
107	A	110	GLN	0	0.006	-0.019	13.961	0.055	0.055	0.000	0.000	0.000	0.000
108	A	111	THR	0	-0.041	-0.019	8.462	-0.430	-0.430	0.000	0.000	0.000	0.000
109	A	112	VAL	0	0.014	0.010	7.529	0.242	0.242	0.000	0.000	0.000	0.000
110	A	113	ILE	0	-0.015	0.005	8.153	-0.272	-0.272	0.000	0.000	0.000	0.000
111	A	114	ASP	-1	-0.771	-0.867	6.869	-1.664	-1.664	0.000	0.000	0.000	0.000
112	A	115	ALA	0	0.015	0.011	10.008	0.223	0.223	0.000	0.000	0.000	0.000
113	A	116	SER	0	-0.009	-0.023	6.022	0.437	0.437	0.000	0.000	0.000	0.000
114	A	117	LYS	1	0.818	0.908	5.394	3.589	3.589	0.000	0.000	0.000	0.000
115	A	118	SER	0	-0.020	-0.014	8.751	-0.066	-0.066	0.000	0.000	0.000	0.000
116	A	119	ILE	0	0.000	-0.004	10.813	-0.043	-0.043	0.000	0.000	0.000	0.000
117	A	120	PHE	0	-0.016	0.001	13.978	0.037	0.037	0.000	0.000	0.000	0.000
118	A	121	VAL	0	0.002	-0.010	17.242	-0.054	-0.054	0.000	0.000	0.000	0.000
119	A	122	PRO	0	-0.005	0.006	19.512	0.022	0.022	0.000	0.000	0.000	0.000
120	A	123	ARG	1	0.909	0.941	22.947	0.038	0.038	0.000	0.000	0.000	0.000
121	A	124	GLY	0	-0.009	-0.020	26.272	0.002	0.002	0.000	0.000	0.000	0.000
122	A	125	VAL	0	-0.044	-0.020	20.349	-0.017	-0.017	0.000	0.000	0.000	0.000
123	A	126	ALA	0	0.003	0.005	23.617	0.011	0.011	0.000	0.000	0.000	0.000
124	A	127	ASN	0	0.015	-0.012	19.323	-0.053	-0.053	0.000	0.000	0.000	0.000
125	A	128	GLY	0	0.038	0.005	19.731	0.046	0.046	0.000	0.000	0.000	0.000
126	A	129	PHE	0	-0.069	-0.029	17.036	-0.057	-0.057	0.000	0.000	0.000	0.000
127	A	130	GLN	0	0.023	0.004	17.195	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	131	VAL	0	-0.053	-0.022	16.506	-0.117	-0.117	0.000	0.000	0.000	0.000
129	A	132	LEU	0	-0.026	-0.008	12.351	-0.017	-0.017	0.000	0.000	0.000	0.000
130	A	133	SER	0	-0.036	-0.032	13.846	-0.048	-0.048	0.000	0.000	0.000	0.000
131	A	134	ASP	-1	-0.847	-0.924	15.645	-0.444	-0.444	0.000	0.000	0.000	0.000
132	A	135	PHE	0	0.008	-0.002	18.097	0.050	0.050	0.000	0.000	0.000	0.000
133	A	136	VAL	0	0.001	0.043	15.367	-0.058	-0.058	0.000	0.000	0.000	0.000
134	A	137	ALA	0	0.005	-0.002	17.633	0.032	0.032	0.000	0.000	0.000	0.000
135	A	138	TYR	0	0.060	0.045	16.795	0.064	0.064	0.000	0.000	0.000	0.000
136	A	139	SER	0	0.004	-0.005	18.258	0.035	0.035	0.000	0.000	0.000	0.000
137	A	140	TYR	0	0.041	0.030	18.575	0.003	0.003	0.000	0.000	0.000	0.000
138	A	141	LEU	0	-0.008	0.016	20.648	0.013	0.013	0.000	0.000	0.000	0.000
139	A	142	VAL	0	-0.013	-0.016	22.596	-0.029	-0.029	0.000	0.000	0.000	0.000
140	A	143	ASN	0	0.016	-0.008	25.384	0.005	0.005	0.000	0.000	0.000	0.000
141	A	144	ASP	-1	-0.799	-0.896	28.077	-0.010	-0.010	0.000	0.000	0.000	0.000
142	A	145	TYR	0	-0.031	-0.014	30.500	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	146	TRP	0	-0.012	-0.006	33.227	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	147	ALA	0	0.037	0.018	34.797	0.007	0.007	0.000	0.000	0.000	0.000
145	A	148	LEU	0	-0.001	-0.004	37.766	-0.008	-0.008	0.000	0.000	0.000	0.000
146	A	149	GLU	-1	-0.907	-0.971	39.242	-0.039	-0.039	0.000	0.000	0.000	0.000
147	A	150	LEU	0	0.017	0.006	33.677	-0.005	-0.005	0.000	0.000	0.000	0.000
148	A	151	LYS	1	0.961	0.996	35.413	0.078	0.078	0.000	0.000	0.000	0.000
149	A	152	PRO	0	-0.080	-0.056	36.411	-0.010	-0.010	0.000	0.000	0.000	0.000
150	A	153	LYS	1	0.785	0.884	34.241	0.072	0.072	0.000	0.000	0.000	0.000
151	A	154	TYR	0	-0.029	-0.018	30.136	0.002	0.002	0.000	0.000	0.000	0.000
152	A	155	ALA	0	-0.032	-0.005	30.058	0.003	0.003	0.000	0.000	0.000	0.000
153	A	156	PHE	0	-0.021	-0.019	28.745	-0.003	-0.003	0.000	0.000	0.000	0.000
154	A	157	VAL	0	-0.001	0.007	26.186	0.008	0.008	0.000	0.000	0.000	0.000
155	A	158	ASN	0	-0.049	-0.030	27.497	-0.036	-0.036	0.000	0.000	0.000	0.000
156	A	159	TYR	0	-0.026	-0.050	23.889	-0.034	-0.034	0.000	0.000	0.000	0.000
157	A	160	ALA	0	0.037	0.033	24.451	-0.044	-0.044	0.000	0.000	0.000	0.000
158	A	161	ASP	-1	-0.789	-0.863	26.968	-0.298	-0.298	0.000	0.000	0.000	0.000
159	A	162	PRO	0	-0.033	-0.020	26.549	-0.024	-0.024	0.000	0.000	0.000	0.000
160	A	163	SER	0	-0.133	-0.089	27.191	-0.007	-0.007	0.000	0.000	0.000	0.000
161	A	164	LEU	0	0.022	0.017	23.731	0.000	0.000	0.000	0.000	0.000	0.000
162	A	165	ASP	-1	-0.885	-0.931	20.672	-0.653	-0.653	0.000	0.000	0.000	0.000
163	A	166	ILE	0	-0.018	-0.001	18.941	-0.058	-0.058	0.000	0.000	0.000	0.000
164	A	167	LYS	1	0.811	0.893	17.960	0.683	0.683	0.000	0.000	0.000	0.000
165	A	168	TRP	0	0.024	-0.005	17.923	-0.081	-0.081	0.000	0.000	0.000	0.000
166	A	169	GLU	-1	-0.850	-0.930	13.523	-1.437	-1.437	0.000	0.000	0.000	0.000
167	A	170	ASN	0	-0.029	-0.026	17.455	0.044	0.044	0.000	0.000	0.000	0.000
168	A	171	LEU	0	0.034	0.030	21.120	0.018	0.018	0.000	0.000	0.000	0.000
169	A	172	GLU	-1	-0.908	-0.958	24.056	-0.488	-0.488	0.000	0.000	0.000	0.000
170	A	173	GLU	-1	-0.920	-0.948	24.499	-0.432	-0.432	0.000	0.000	0.000	0.000
171	A	174	ALA	0	-0.028	-0.003	24.105	-0.003	-0.003	0.000	0.000	0.000	0.000
172	A	175	GLU	-1	-0.779	-0.865	24.829	-0.238	-0.238	0.000	0.000	0.000	0.000
173	A	176	VAL	0	0.021	0.009	25.821	-0.017	-0.017	0.000	0.000	0.000	0.000
174	A	177	SER	0	-0.076	-0.059	28.022	0.030	0.030	0.000	0.000	0.000	0.000
175	A	178	GLU	-1	-0.847	-0.948	30.630	-0.192	-0.192	0.000	0.000	0.000	0.000
176	A	179	ALA	0	-0.047	-0.012	31.933	0.005	0.005	0.000	0.000	0.000	0.000
177	A	180	ASP	-1	-0.761	-0.867	27.690	-0.268	-0.268	0.000	0.000	0.000	0.000
178	A	181	GLU	-1	-0.804	-0.886	29.756	-0.306	-0.306	0.000	0.000	0.000	0.000
179	A	182	ASN	0	-0.106	-0.058	31.634	0.005	0.005	0.000	0.000	0.000	0.000
180	A	183	HIS	0	-0.039	0.006	28.697	0.024	0.024	0.000	0.000	0.000	0.000
181	A	184	PRO	0	0.001	0.006	32.562	-0.006	-0.006	0.000	0.000	0.000	0.000
182	A	185	PHE	0	0.060	0.021	31.119	-0.019	-0.019	0.000	0.000	0.000	0.000
183	A	186	LEU	0	0.058	0.020	27.461	0.018	0.018	0.000	0.000	0.000	0.000
184	A	187	LYS	1	0.771	0.864	30.842	0.213	0.213	0.000	0.000	0.000	0.000
185	A	188	ASP	-1	-0.844	-0.902	34.216	-0.180	-0.180	0.000	0.000	0.000	0.000
186	A	189	VAL	0	-0.038	-0.004	30.598	0.012	0.012	0.000	0.000	0.000	0.000
187	A	190	LYS	1	0.822	0.900	33.723	0.125	0.125	0.000	0.000	0.000	0.000
188	A	191	PRO	0	-0.003	0.005	31.842	0.000	0.000	0.000	0.000	0.000	0.000
189	A	192	LEU	0	0.012	0.024	29.275	0.016	0.016	0.000	0.000	0.000	0.000
190	A	193	ARG	1	0.855	0.914	32.203	0.083	0.083	0.000	0.000	0.000	0.000
191	A	194	LYS	1	0.930	0.952	30.704	0.106	0.106	0.000	0.000	0.000	0.000
192	A	195	GLU	-1	-0.800	-0.881	34.757	-0.069	-0.069	0.000	0.000	0.000	0.000
193	A	196	ASP	-1	-0.808	-0.882	33.839	-0.091	-0.091	0.000	0.000	0.000	0.000
194	A	197	LEU	0	-0.028	0.012	29.061	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASN)